DH12B_DANRE
ID DH12B_DANRE Reviewed; 311 AA.
AC Q6QA33; Q6PBR0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Very-long-chain 3-oxoacyl-CoA reductase-B {ECO:0000305};
DE EC=1.1.1.330 {ECO:0000250|UniProtKB:Q53GQ0};
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 12-B {ECO:0000250|UniProtKB:Q53GQ0};
DE Short=17-beta-HSD 12-B {ECO:0000250|UniProtKB:Q53GQ0};
DE Short=zf3.3;
DE Short=zfHSD17B12B;
DE AltName: Full=3-ketoacyl-CoA reductase {ECO:0000250|UniProtKB:Q53GQ0};
DE Short=KAR {ECO:0000250|UniProtKB:Q53GQ0};
DE AltName: Full=Estradiol 17-beta-dehydrogenase 12-B {ECO:0000250|UniProtKB:Q53GQ0};
DE EC=1.1.1.62 {ECO:0000250|UniProtKB:Q53GQ0};
GN Name=hsd17b12b; ORFNames=zgc:73289;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=15026171; DOI=10.1016/j.mce.2003.11.010;
RA Mindnich R., Deluca D., Adamski J.;
RT "Identification and characterization of 17 beta-hydroxysteroid
RT dehydrogenases in the zebrafish, Danio rerio.";
RL Mol. Cell. Endocrinol. 215:19-30(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the second of the four reactions of the long-chain
CC fatty acids elongation cycle. This endoplasmic reticulum-bound
CC enzymatic process, allows the addition of two carbons to the chain of
CC long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has
CC a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-
CC hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby,
CC it may participate in the production of VLCFAs of different chain
CC lengths that are involved in multiple biological processes as
CC precursors of membrane lipids and lipid mediators. May also catalyze
CC the transformation of estrone (E1) into estradiol (E2) and play a role
CC in estrogen formation. {ECO:0000250|UniProtKB:Q53GQ0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-
CC long-chain 3-oxoacyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:48680,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:85440, ChEBI:CHEBI:90725; EC=1.1.1.330;
CC Evidence={ECO:0000250|UniProtKB:Q53GQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH;
CC Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62;
CC Evidence={ECO:0000250|UniProtKB:Q53GQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH;
CC Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.62;
CC Evidence={ECO:0000250|UniProtKB:Q53GQ0};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q53GQ0}.
CC -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC {ECO:0000250|UniProtKB:Q53GQ0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q53GQ0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q53GQ0}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development. Weakly or not
CC expressed in some adult organs. {ECO:0000269|PubMed:15026171}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. 17-beta-HSD 3 subfamily. {ECO:0000305}.
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DR EMBL; AY551080; AAS58450.1; -; mRNA.
DR EMBL; BC059617; AAH59617.1; -; mRNA.
DR RefSeq; NP_955907.1; NM_199613.1.
DR AlphaFoldDB; Q6QA33; -.
DR SMR; Q6QA33; -.
DR STRING; 7955.ENSDARP00000089612; -.
DR PaxDb; Q6QA33; -.
DR Ensembl; ENSDART00000098842; ENSDARP00000089612; ENSDARG00000035872.
DR GeneID; 322626; -.
DR KEGG; dre:322626; -.
DR CTD; 322626; -.
DR ZFIN; ZDB-GENE-030131-1346; hsd17b12b.
DR eggNOG; KOG1014; Eukaryota.
DR GeneTree; ENSGT00940000154860; -.
DR HOGENOM; CLU_010194_38_0_1; -.
DR InParanoid; Q6QA33; -.
DR OMA; TIAPMMV; -.
DR OrthoDB; 895581at2759; -.
DR PhylomeDB; Q6QA33; -.
DR TreeFam; TF314591; -.
DR UniPathway; UPA00094; -.
DR UniPathway; UPA00769; -.
DR PRO; PR:Q6QA33; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000035872; Expressed in liver and 26 other tissues.
DR ExpressionAtlas; Q6QA33; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0102339; F:3-oxo-arachidoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102340; F:3-oxo-behenoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102342; F:3-oxo-cerotoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102341; F:3-oxo-lignoceroyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006703; P:estrogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW NADP; Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..311
FT /note="Very-long-chain 3-oxoacyl-CoA reductase-B"
FT /id="PRO_0000248372"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 48..77
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="E -> D (in Ref. 1; AAS58450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 34279 MW; 995F46371555BFB4 CRC64;
MEPFADALFW VGAVTVLWLS VSSLWSLING IRVWILGNGN LMRASSLGKW AVVTGATDGI
GKAYAEELAR RGFAIVLISR TQEKLDEVSK AIESKYKVET KTISADFGSV DIYPKIESGL
AGLEIGVLVN NVGVSYSYPE FFLNIPDVDS FINNMININI MSVCQMTRLV LPRMVDRSKG
VILNVASASG MYPVPLLTLY SSTKAFVDFF SRGLDAEYKS KGIIIQSVLP FYVTTKLSKI
RKPTLDIPTP ERYVKAQLST IGLQTQSNGY LPHAIMGWVT ASLLPAKLLN KYVMGMGLSQ
RARYLKKQKQ G
